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Biotinylated Musa Paradisiaca (Banana) Lectin

Catalog Number: B-1415

Availability: In stock

$100.00
Unit Size: 2 mg

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Overview

    Isolated from the cultivated banana Musa paradisiaca, banana lectin (BanLec) is a very stable mannose- and glucose-binding lectin consisting of two identical 15 kDa subunits and a reported isoelectric point of pH 7.3. Although structurally related to the Jacalin family of lectins, BanLec recognizes internal α(1,3) glucosyl- and mannosyl- residues and has also been reported to bind β(1,3) and β(1,6) glucosyl-structures.

    Like Galanthus nivalis lectin, BanLec has been shown to bind gp 120 glycoprotein, an important envelope component of the human immunodeficiency virus (HIV-1), and to strongly inhibit HIV-1 entry into cells. Glycoproteins on the surface of other viruses are also likely to be recognizable by BanLec. This lectin has been reported to be a potent mitogen for peripheral T-cells in the presence of interleukin-2, and appears likely to be a cause of allergic reaction to bananas, since IgG4 antibodies against BanLec have been detected in humans.

    Biotinylated BanLec has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide.

    Additional Information

    Catalog Number B-1415
    Unit Size 2 mg
    Country of Manufacture United States
    Applications Immunohistochemistry / Immunocytochemistry, Immunofluorescence, Blotting Applications, Elispot, ELISAs, Glycobiology
    Conjugate Biotinylated
    Sugar Specificity Mannose, Glucose
Additional Info

    Details

    Isolated from the cultivated banana Musa paradisiaca, banana lectin (BanLec) is a very stable mannose- and glucose-binding lectin consisting of two identical 15 kDa subunits and a reported isoelectric point of pH 7.3. Although structurally related to the Jacalin family of lectins, BanLec recognizes internal α(1,3) glucosyl- and mannosyl- residues and has also been reported to bind β(1,3) and β(1,6) glucosyl-structures.

    Like Galanthus nivalis lectin, BanLec has been shown to bind gp 120 glycoprotein, an important envelope component of the human immunodeficiency virus (HIV-1), and to strongly inhibit HIV-1 entry into cells. Glycoproteins on the surface of other viruses are also likely to be recognizable by BanLec. This lectin has been reported to be a potent mitogen for peripheral T-cells in the presence of interleukin-2, and appears likely to be a cause of allergic reaction to bananas, since IgG4 antibodies against BanLec have been detected in humans.

    Biotinylated BanLec has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. This conjugate is supplied essentially free of unconjugated biotins and is preserved with sodium azide.

    This biotinylated lectin is an ideal intermediate for examining glycoconjugates using the Biotin-Avidin/Streptavidin System. First the biotinylated lectin is added, followed by the VECTASTAIN ABC Reagent, Avidin D conjugate, or streptavidin derivative.

    Inhibiting/eluting sugar: 200 mM α-methyl mannoside or mannose
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